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Information on EC 1.14.14.84 - linalool 8-monooxygenase
for references in articles please use BRENDA:EC1.14.14.84
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.84 linalool 8-monooxygenase
IUBMB Comments
A cytochrome P-450 (heme-thiolate) protein found in plants. The secondary electron donor is a specific [2Fe-2S] ferredoxin from the same bacterial strain.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
cytochrome p450lin, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cytochrome P-450 linalool 8-hydroxylase
cytochrome P-450-dependent linalool 8-hydroxylase
Cytochrome P450 111
-
-
-
-
Cytochrome P450lin
-
-
-
-
EC 1.14.13.151
-
-
formerly
-
EC 1.14.99.28
-
-
formerly
-
LIN reductase
linalool-8-monooxygenase
-
-
-
-
oxygenase, linalool 8-mono-
-
-
-
-
P45O1in
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(6E)-8-hydroxylinalool + [reduced NADPH-hemoprotein reductase] + O2 = (6E)-8-oxolinalool + [oxidized NADPH-hemoprotein reductase] + 2 H2O
1b
-
-
-
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = (6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
linalool + [reduced NADPH-hemoprotein reductase] + O2 = (6E)-8-hydroxylinalool + [oxidized NADPH-hemoprotein reductase] + H2O
1a
-
-
-
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = (6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
mixed function monooxygenase consisting of LIN-reductase, Fe2S2-redoxin and cytochrome LIN P-450
-
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = (6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
overall reaction
-
-
-
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = (6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
mixed function monooxygenase consisting of LIN-reductase, Fe2S2-redoxin and cytochrome LIN P-450
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
linalool,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (8-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein found in plants. The secondary electron donor is a specific [2Fe-2S] ferredoxin from the same bacterial strain.
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CAS REGISTRY NUMBER
COMMENTARY
95329-13-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(6E)-8-hydroxylinalool + [reduced NADPH-hemoprotein reductase] + O2
(6E)-8-oxolinalool + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: product analysis by mass spectrometry
Products: product analysis by mass spectrometry
?
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [reduced NADPH-hemoprotein reductase] + O2
8-oxolinalool + [oxidized NADPH-hemoprotein reductase] + H2O
3,7-dimethylocta-1,6-dien-3-ol + [reduced NADPH-hemoprotein reductase] + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [oxidized NADPH-hemoprotein reductase] + H2O
6-methyl-hex-5-en-2-ol + [reduced NADPH-hemoprotein reductase] + O2
6-methyl-hex-5-en-2-one + [oxidized NADPH-hemoprotein reductase] + H2O
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
linalool + NADH + O2
(6E)-8-hydroxylinalool + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
r
linalool + [reduced NADPH-hemoprotein reductase] + O2
(6E)-8-hydroxylinalool + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: product analysis by mass spectrometry
Products: product analysis by mass spectrometry
?
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [reduced NADPH-hemoprotein reductase] + O2
8-oxolinalool + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: 8-hydroxylinalool
Products: -
Products: -
?
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [reduced NADPH-hemoprotein reductase] + O2
8-oxolinalool + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: 8-hydroxylinalool
Products: -
Products: -
?
3,7-dimethylocta-1,6-dien-3-ol + [reduced NADPH-hemoprotein reductase] + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: 8-hydroxylinalool
Products: 8-hydroxylinalool
?
3,7-dimethylocta-1,6-dien-3-ol + [reduced NADPH-hemoprotein reductase] + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: both isomers of linalool, strict substrate specificity: geraniol, nerol or citronellol are not hydroxylated
Products: -
Products: -
?
3,7-dimethylocta-1,6-dien-3-ol + [reduced NADPH-hemoprotein reductase] + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: linalool, initial reaction in linalool catabolism
Products: -
Products: -
?
3,7-dimethylocta-1,6-dien-3-ol + [reduced NADPH-hemoprotein reductase] + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: both isomers of linalool, strict substrate specificity: geraniol, nerol or citronellol are not hydroxylated
Products: -
Products: -
?
3,7-dimethylocta-1,6-dien-3-ol + [reduced NADPH-hemoprotein reductase] + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: 8-hydroxylinalool
Products: 8-hydroxylinalool
?
3,7-dimethylocta-1,6-dien-3-ol + [reduced NADPH-hemoprotein reductase] + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: linalool, initial reaction in linalool catabolism
Products: -
Products: -
?
6-methyl-hex-5-en-2-ol + [reduced NADPH-hemoprotein reductase] + O2
6-methyl-hex-5-en-2-one + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
ir
6-methyl-hex-5-en-2-ol + [reduced NADPH-hemoprotein reductase] + O2
6-methyl-hex-5-en-2-one + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
ir
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: NMR spectroscopy product analysis
Products: NMR spectroscopy product analysis
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: overall reaction
Products: product analysis by mass spectrometry
Products: product analysis by mass spectrometry
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: overview: synthetic analogues of linalool
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not perform 10-methyl hydroxylation of linalool
Products: -
Products: -
?
additional information
?
-
-
Substrates: overview: synthetic analogues of linalool
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not perform 10-methyl hydroxylation of linalool
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,7-dimethylocta-1,6-dien-3-ol + [reduced NADPH-hemoprotein reductase] + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [oxidized NADPH-hemoprotein reductase] + H2O
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
3,7-dimethylocta-1,6-dien-3-ol + [reduced NADPH-hemoprotein reductase] + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: linalool, initial reaction in linalool catabolism
Products: -
Products: -
?
3,7-dimethylocta-1,6-dien-3-ol + [reduced NADPH-hemoprotein reductase] + O2
(E)-3,7-dimethylocta-1,6-dien-3,8-diol + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: linalool, initial reaction in linalool catabolism
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
-
Substrates: -
Products: -
Products: -
?
linalool + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(6E)-8-oxolinalool + 2 [oxidized NADPH-hemoprotein reductase] + 3 H2O
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
-
requirement of two enzyme components, iron-heme protein and iron-sulfur protein
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
overview: values for cytochrome LIN P-450 with various synthetic substrates
-
2
NADH
-
substrate-stimulated NADH oxidation using excess amounts of P-450 and FAD component of the enzyme
32
NADH
-
substrate-stimulated NADH oxidation using excess amounts of iron-sulfur and FAD component of the enzyme
43
NADH
-
substrate-stimulated NADH oxidation using excess amounts of iron sulfur and P-450 component of the enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.014
-
purified enzyme, pH 7.4, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
strain PpG777 utilizes linalool as sole carbon and energy source
brenda
additional information
-
strain PpG777 utilizes linalool as sole carbon and energy source
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
P45O1in is a member of the CYPIll P-450 monooxygenase gene family
evolution
-
the enzyme belongs to the CYP111 family of heme-dependent cytochrome P450 monooxygenases
evolution
-
the enzyme belongs to the CYP111 family of heme-dependent cytochrome P450 monooxygenases
-
evolution
-
P45O1in is a member of the CYPIll P-450 monooxygenase gene family
-
metabolism
P-4501in catalyzes the 8-methyl hydroxylation of linalool as the first committed step of its utilization by Pseudomonas putida as the sole carbon source
metabolism
-
P-4501in catalyzes the 8-methyl hydroxylation of linalool as the first committed step of its utilization by Pseudomonas putida as the sole carbon source
-
additional information
-
analysis of the heme-thiolate reaction center, molecular domains of substrate specificity, redox-pair interactions, and the regulation of the reaction cycle, overview
additional information
P-4501in exhibits conservation in the axial cysteine heme ligand-containing peptide and the threonine region postulated to form an 02-binding pocket
additional information
-
analysis of the heme-thiolate reaction center, molecular domains of substrate specificity, redox-pair interactions, and the regulation of the reaction cycle, overview
-
additional information
-
P-4501in exhibits conservation in the axial cysteine heme ligand-containing peptide and the threonine region postulated to form an 02-binding pocket
-
Show AA Sequence and Transmembrane Helices (324 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
multi-component enzyme consisting of LIN-reductase, Fe2-S2-redoxin and cytochrome LIN-P450. MW of the reductase: 43700 Da, analytical data from amino acid composition and prosthetic group quantification, 45000 Da, gel filtration. MW of Fe2-S2-redoxin: 11000 Da, gel filtration, 12800 Da, analytical data from amino acid composition and prosthetic group quantification. MW of cytochrome LIN-P450: 44800 Da, analytical data from amino acid composition and prosthetic group quantification, 45000 Da, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
-
enzyme consists of LIN-reductase, MW 44000 Da, and Fe2S2-redoxin, MW 10700 Da, and cytochrome LIN-P450, MW 47000 Da, SDS-PAGE
additional information
-
enzyme consists of LIN-reductase, MW 44000 Da, and Fe2S2-redoxin, MW 10700 Da, and cytochrome LIN-P450, MW 47000 Da, SDS-PAGE
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
interaction and coupling of CYP enzyme reactions from Novosphingobium aromaticivorans with ferredoxin reductases ArR from Novosphingobium aromaticivorans and PdR from from Rhodopseudomonas palustris CGA009, activity reconstitution with the electron transfer system of ArR and Arx, overview
additional information
-
interaction and coupling of CYP enzyme reactions from Novosphingobium aromaticivorans with ferredoxin reductases ArR from Novosphingobium aromaticivorans and PdR from from Rhodopseudomonas palustris CGA009, activity reconstitution with the electron transfer system of ArR and Arx, overview
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196°C, LIN-redoxin reductase and cytochrome LINP-450 in solution stable over a long period after ultrafiltration or dialysis and repeated freeze/thaw-cycles
-
0°C, LIN-redoxin loses its prosthetic group, 5 mM DTT retards apoprotein formation
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by anion exchange chromatography, ammonium sulfate fractionation, a second step of anion exchange chromatography, affinity chromatography, a thrid step of anion exchange chromatography, and two further different steps of affinity chromatography to over 90% hommogeneity
-
recombinant enzyme from Escherichia coli by anion exchange chromatography, ammonium sulfate fractionation, gel filtration, and a second step of anion exchange chromatography
recombinant enzyme from Escherichia coli by ultrafiltration and anion exchange chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CYP111A2 cloning, expression in Escherichia coli strain DH5alpha
-
gene linC, DNA and amino acid sequence determination and analysis, constitutive functional expression in Escherichia coli from plasmid pUC18 under control of the lac promoter
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bhattacharyya, P.K.; Samanta, T.B.; Ullah, A.H.J.; Gunsalus, I.C.
Chemical probes into the active centre of a heme thiolate monoxygenase
Proc. Indian Acad. Sci. Chem. Sci.
93
1289-1304
1984
Pseudomonas putida, Pseudomonas putida PpG777
-
brenda
Ullah, A.H.J.; Murray, R.I.; Bhattacharyya, P.K.; Wagner, G.C.; Gunsalus, I.C.
Protein components of a cytochrome P-450 linalool 8-methyl hydroxylase
J. Biol. Chem.
265
1345-1351
1990
Pseudomonas putida, Pseudomonas putida PpG777
brenda
Bernhardt, R.; Gunsalus I.C.
Reconstitution of cytochrome P4502B4 (LM2) activity with camphor and linalool monooxygenase electron donors
Biochem. Biophys. Res. Commun.
187
310-317
1992
Pseudomonas putida
brenda
Bell, S.G.; Dale, A.; Rees, N.H.; Wong, L.L.
A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans
Appl. Microbiol. Biotechnol.
86
163-175
2010
Novosphingobium aromaticivorans, Novosphingobium aromaticivorans ATCC 700278D-5
brenda
Ropp, J.; Gunsalus, I.; Sligar, S.
Cloning and expression of a member of a new cytochrome P-450 family: Cytochrome P-450lin (CYP111) from Pseudomonas incognita
J. Bacteriol.
175
6028-6037
1993
Pseudomonas putida (Q59723), Pseudomonas putida PpG777 (Q59723)
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.14.84)
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